Title |
Dominant-negative activity of the STAT3-Y705F mutant depends on the N-terminal domain
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Published in |
Cell Communication and Signaling, November 2013
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DOI | 10.1186/1478-811x-11-83 |
Pubmed ID | |
Authors |
Anne Mohr, Dirk Fahrenkamp, Natalie Rinis, Gerhard Müller-Newen |
Abstract |
STAT3 is a transcription factor of central importance in chronic inflammation and cancer. In response to cytokine stimulation STAT3 is phosphorylated on a single tyrosine residue at position 705, dimerizes and accumulates in the nucleus to induce target gene expression. The substitution of tyrosine 705 to phenylalanine leads to a dominant-negative STAT3 mutant (STAT3-YF) which influences the activation of WT-STAT3 in stimulated cells through a mechanism that is not completely understood. In this study we analyzed the molecular mechanism of STAT3-YF dominant-negative activity in IL-6-induced STAT3 signaling and the relevance of the N-terminal domain. |
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